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Purification and characterization of a human brain galectin-1 ligand.

Authors :
Chadli A
LeCaer JP
Bladier D
Joubert-Caron R
Caron M
Source :
Journal of neurochemistry [J Neurochem] 1997 Apr; Vol. 68 (4), pp. 1640-7.
Publication Year :
1997

Abstract

Our previous studies have characterized an endogenous lectin from human brain identified as galectin-1. A soluble ligand of galectin-1 was purified from human brain by affinity chromatography and preparative electrophoresis. The purified ligand (termed HBGp82, for human brain galectin-1-binding polypeptide of 82,000 daltons) has an apparent molecular mass of 82 kDa and is glycosylated by N-linked biantennary complex structures. HBGp82 was partially characterized by microsequencing of peptide fragments. Similar peptides were found in a heat shock of protein of 90,000 daltons, hsp90. However, comparison of apparent molecular weights and matrix-assisted laser desorption mass spectrometry clearly showed that HBGp82 differs to some degree from hsp90.

Details

Language :
English
ISSN :
0022-3042
Volume :
68
Issue :
4
Database :
MEDLINE
Journal :
Journal of neurochemistry
Publication Type :
Academic Journal
Accession number :
9084436
Full Text :
https://doi.org/10.1046/j.1471-4159.1997.68041640.x